HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 19-JAN-08 3C0B
TITLE CRYSTAL STRUCTURE OF THE CONSERVED ARCHAEAL PROTEIN Q6M145. NORTHEAST
TITLE 2 STRUCTURAL GENOMICS CONSORTIUM TARGET MRR63
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONSERVED ARCHAEAL PROTEIN Q6M145;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOCOCCUS MARIPALUDIS S2;
SOURCE 3 ORGANISM_TAXID: 267377;
SOURCE 4 STRAIN: S2 / LL;
SOURCE 5 GENE: MMP0072;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS XRAY, MRR63, NESG, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, UNKNOWN
KEYWDS 3 FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.P.KUZIN,M.SU,J.SEETHARAMAN,D.WANG,Y.FANG,K.CUNNINGHAM,L.-C.MA,
AUTHOR 2 R.XIAO,J.LIU,M.C.BARAN,T.B.ACTON,B.ROST,G.T.MONTELIONE,J.F.HUNT,
AUTHOR 3 L.TONG,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 5 20-OCT-21 3C0B 1 REMARK SEQADV LINK
REVDAT 4 24-JAN-18 3C0B 1 AUTHOR JRNL
REVDAT 3 25-OCT-17 3C0B 1 REMARK
REVDAT 2 24-FEB-09 3C0B 1 VERSN
REVDAT 1 26-FEB-08 3C0B 0
JRNL AUTH A.P.KUZIN,M.SU,J.SEETHARAMAN,D.WANG,Y.FANG,K.CUNNINGHAM,
JRNL AUTH 2 L.-C.MA,R.XIAO,J.LIU,M.C.BARAN,T.B.ACTON,B.ROST,
JRNL AUTH 3 G.T.MONTELIONE,J.F.HUNT,L.TONG
JRNL TITL X-RAY STRUCTURE OF THE CONSERVED ARCHAEAL PROTEIN Q6M145.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 130737.100
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 109470
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5442
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 15076
REMARK 3 BIN R VALUE (WORKING SET) : 0.2300
REMARK 3 BIN FREE R VALUE : 0.2650
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 778
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.009
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9750
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 160
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.91200
REMARK 3 B22 (A**2) : -3.17900
REMARK 3 B33 (A**2) : -2.73300
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -7.43600
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.19
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.25
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.740
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 35.29
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE FRIEDEL PAIRS WERE USED IN PHASING.
REMARK 3 BULK SOLVENT MODEL USED IN REFINEMENT
REMARK 4
REMARK 4 3C0B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-08.
REMARK 100 THE DEPOSITION ID IS D_1000046180.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-OCT-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.15
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97900
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 121560
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.34200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SNB
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE STRUCTURE FACTOR FILE CONTAINS FRIEDEL PAIRS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 400, 0.1M CALCIUM ACETATE,
REMARK 280 0.1M MES, PH 6.15, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 78.70000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.63300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 78.70000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 43.63300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2770 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 78.70000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 43.63300
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2800 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 TRP A 33
REMARK 465 LYS A 34
REMARK 465 ASN A 35
REMARK 465 ASN A 36
REMARK 465 LEU A 61
REMARK 465 ALA A 62
REMARK 465 ASP A 63
REMARK 465 SER A 64
REMARK 465 TYR A 65
REMARK 465 GLU A 66
REMARK 465 THR A 67
REMARK 465 LYS A 68
REMARK 465 LYS A 69
REMARK 465 ASN A 106
REMARK 465 MSE A 107
REMARK 465 HIS A 332
REMARK 465 HIS A 333
REMARK 465 HIS A 334
REMARK 465 PRO B 31
REMARK 465 MSE B 32
REMARK 465 TRP B 33
REMARK 465 LYS B 34
REMARK 465 LEU B 61
REMARK 465 ALA B 62
REMARK 465 ASP B 63
REMARK 465 SER B 64
REMARK 465 TYR B 65
REMARK 465 GLU B 66
REMARK 465 THR B 67
REMARK 465 LYS B 68
REMARK 465 LYS B 69
REMARK 465 HIS B 332
REMARK 465 HIS B 333
REMARK 465 HIS B 334
REMARK 465 TRP C 33
REMARK 465 LYS C 34
REMARK 465 ASN C 35
REMARK 465 ASN C 36
REMARK 465 LEU C 61
REMARK 465 ALA C 62
REMARK 465 ASP C 63
REMARK 465 SER C 64
REMARK 465 TYR C 65
REMARK 465 GLU C 66
REMARK 465 THR C 67
REMARK 465 LYS C 68
REMARK 465 LYS C 69
REMARK 465 HIS C 331
REMARK 465 HIS C 332
REMARK 465 HIS C 333
REMARK 465 HIS C 334
REMARK 465 TRP D 33
REMARK 465 LYS D 34
REMARK 465 ASN D 35
REMARK 465 ASN D 36
REMARK 465 THR D 58
REMARK 465 ALA D 59
REMARK 465 GLU D 60
REMARK 465 LEU D 61
REMARK 465 ALA D 62
REMARK 465 ASP D 63
REMARK 465 SER D 64
REMARK 465 TYR D 65
REMARK 465 GLU D 66
REMARK 465 THR D 67
REMARK 465 LYS D 68
REMARK 465 LYS D 69
REMARK 465 HIS D 330
REMARK 465 HIS D 331
REMARK 465 HIS D 332
REMARK 465 HIS D 333
REMARK 465 HIS D 334
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 43 57.47 -141.17
REMARK 500 ASN A 48 -75.97 -92.44
REMARK 500 THR A 57 -130.45 -105.76
REMARK 500 THR A 58 -76.93 -121.25
REMARK 500 ALA A 59 91.84 65.05
REMARK 500 PHE A 83 16.83 -142.28
REMARK 500 ALA A 111 -169.83 -164.00
REMARK 500 LEU A 170 -61.34 -126.55
REMARK 500 ARG A 171 46.49 -93.76
REMARK 500 CYS A 215 160.85 -46.90
REMARK 500 LYS A 221 -169.69 -114.50
REMARK 500 LYS A 225 -70.46 -59.57
REMARK 500 ALA A 312 36.68 -145.82
REMARK 500 HIS A 330 71.98 -105.27
REMARK 500 VAL B 56 -171.92 -61.34
REMARK 500 THR B 57 -156.93 -127.95
REMARK 500 ALA B 59 99.39 -54.31
REMARK 500 ASN B 86 49.44 -81.87
REMARK 500 SER B 101 -85.37 23.46
REMARK 500 ALA B 102 -79.91 -15.54
REMARK 500 THR B 104 -14.04 -46.69
REMARK 500 ASN B 105 66.32 -102.74
REMARK 500 ASN B 106 -96.72 12.54
REMARK 500 MSE B 107 141.80 -35.03
REMARK 500 LYS B 108 -17.30 102.26
REMARK 500 SER B 110 144.22 -37.77
REMARK 500 CYS B 129 -171.03 -172.63
REMARK 500 LEU B 170 -52.99 -132.95
REMARK 500 ASP B 224 170.44 -54.19
REMARK 500 ALA B 312 36.33 -146.87
REMARK 500 HIS B 330 -96.95 -95.25
REMARK 500 PHE C 30 164.18 174.43
REMARK 500 THR C 58 -85.12 -64.47
REMARK 500 ALA C 59 41.79 75.61
REMARK 500 GLU C 100 -163.33 -67.63
REMARK 500 SER C 101 -101.73 16.36
REMARK 500 ALA C 102 -76.46 -3.72
REMARK 500 ILE C 125 -56.11 -121.16
REMARK 500 TYR C 166 59.38 -90.74
REMARK 500 GLU C 211 4.64 -68.82
REMARK 500 GLU C 328 31.80 -92.77
REMARK 500 VAL D 42 12.14 -60.60
REMARK 500 LEU D 43 38.44 -144.32
REMARK 500 ASN D 74 0.58 -68.46
REMARK 500 PHE D 83 -9.44 -140.10
REMARK 500 ASN D 86 46.63 -95.85
REMARK 500 ASP D 91 170.85 -55.21
REMARK 500 THR D 104 69.89 -67.66
REMARK 500 ASN D 105 115.68 63.50
REMARK 500 SER D 110 96.66 -56.47
REMARK 500
REMARK 500 THIS ENTRY HAS 52 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MRR63 RELATED DB: TARGETDB
DBREF 3C0B A 1 326 UNP Q6M145 Q6M145_METMP 1 326
DBREF 3C0B B 1 326 UNP Q6M145 Q6M145_METMP 1 326
DBREF 3C0B C 1 326 UNP Q6M145 Q6M145_METMP 1 326
DBREF 3C0B D 1 326 UNP Q6M145 Q6M145_METMP 1 326
SEQADV 3C0B ASN A 48 UNP Q6M145 LYS 48 ENGINEERED MUTATION
SEQADV 3C0B VAL A 50 UNP Q6M145 ILE 50 ENGINEERED MUTATION
SEQADV 3C0B ASN A 93 UNP Q6M145 ASP 93 ENGINEERED MUTATION
SEQADV 3C0B SER A 101 UNP Q6M145 GLY 101 ENGINEERED MUTATION
SEQADV 3C0B ASN A 106 UNP Q6M145 TYR 106 ENGINEERED MUTATION
SEQADV 3C0B GLU A 146 UNP Q6M145 ASP 146 ENGINEERED MUTATION
SEQADV 3C0B SER A 182 UNP Q6M145 LEU 182 ENGINEERED MUTATION
SEQADV 3C0B ASP A 187 UNP Q6M145 ASN 187 ENGINEERED MUTATION
SEQADV 3C0B ASN A 254 UNP Q6M145 THR 254 ENGINEERED MUTATION
SEQADV 3C0B GLU A 268 UNP Q6M145 LYS 268 ENGINEERED MUTATION
SEQADV 3C0B ASN A 269 UNP Q6M145 LYS 269 ENGINEERED MUTATION
SEQADV 3C0B LEU A 284 UNP Q6M145 ILE 284 ENGINEERED MUTATION
SEQADV 3C0B ALA A 294 UNP Q6M145 GLY 294 ENGINEERED MUTATION
SEQADV 3C0B LEU A 327 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B GLU A 328 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS A 329 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS A 330 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS A 331 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS A 332 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS A 333 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS A 334 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B ASN B 48 UNP Q6M145 LYS 48 ENGINEERED MUTATION
SEQADV 3C0B VAL B 50 UNP Q6M145 ILE 50 ENGINEERED MUTATION
SEQADV 3C0B ASN B 93 UNP Q6M145 ASP 93 ENGINEERED MUTATION
SEQADV 3C0B SER B 101 UNP Q6M145 GLY 101 ENGINEERED MUTATION
SEQADV 3C0B ASN B 106 UNP Q6M145 TYR 106 ENGINEERED MUTATION
SEQADV 3C0B GLU B 146 UNP Q6M145 ASP 146 ENGINEERED MUTATION
SEQADV 3C0B SER B 182 UNP Q6M145 LEU 182 ENGINEERED MUTATION
SEQADV 3C0B ASP B 187 UNP Q6M145 ASN 187 ENGINEERED MUTATION
SEQADV 3C0B ASN B 254 UNP Q6M145 THR 254 ENGINEERED MUTATION
SEQADV 3C0B GLU B 268 UNP Q6M145 LYS 268 ENGINEERED MUTATION
SEQADV 3C0B ASN B 269 UNP Q6M145 LYS 269 ENGINEERED MUTATION
SEQADV 3C0B LEU B 284 UNP Q6M145 ILE 284 ENGINEERED MUTATION
SEQADV 3C0B ALA B 294 UNP Q6M145 GLY 294 ENGINEERED MUTATION
SEQADV 3C0B LEU B 327 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B GLU B 328 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS B 329 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS B 330 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS B 331 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS B 332 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS B 333 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS B 334 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B ASN C 48 UNP Q6M145 LYS 48 ENGINEERED MUTATION
SEQADV 3C0B VAL C 50 UNP Q6M145 ILE 50 ENGINEERED MUTATION
SEQADV 3C0B ASN C 93 UNP Q6M145 ASP 93 ENGINEERED MUTATION
SEQADV 3C0B SER C 101 UNP Q6M145 GLY 101 ENGINEERED MUTATION
SEQADV 3C0B ASN C 106 UNP Q6M145 TYR 106 ENGINEERED MUTATION
SEQADV 3C0B GLU C 146 UNP Q6M145 ASP 146 ENGINEERED MUTATION
SEQADV 3C0B SER C 182 UNP Q6M145 LEU 182 ENGINEERED MUTATION
SEQADV 3C0B ASP C 187 UNP Q6M145 ASN 187 ENGINEERED MUTATION
SEQADV 3C0B ASN C 254 UNP Q6M145 THR 254 ENGINEERED MUTATION
SEQADV 3C0B GLU C 268 UNP Q6M145 LYS 268 ENGINEERED MUTATION
SEQADV 3C0B ASN C 269 UNP Q6M145 LYS 269 ENGINEERED MUTATION
SEQADV 3C0B LEU C 284 UNP Q6M145 ILE 284 ENGINEERED MUTATION
SEQADV 3C0B ALA C 294 UNP Q6M145 GLY 294 ENGINEERED MUTATION
SEQADV 3C0B LEU C 327 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B GLU C 328 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS C 329 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS C 330 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS C 331 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS C 332 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS C 333 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS C 334 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B ASN D 48 UNP Q6M145 LYS 48 ENGINEERED MUTATION
SEQADV 3C0B VAL D 50 UNP Q6M145 ILE 50 ENGINEERED MUTATION
SEQADV 3C0B ASN D 93 UNP Q6M145 ASP 93 ENGINEERED MUTATION
SEQADV 3C0B SER D 101 UNP Q6M145 GLY 101 ENGINEERED MUTATION
SEQADV 3C0B ASN D 106 UNP Q6M145 TYR 106 ENGINEERED MUTATION
SEQADV 3C0B GLU D 146 UNP Q6M145 ASP 146 ENGINEERED MUTATION
SEQADV 3C0B SER D 182 UNP Q6M145 LEU 182 ENGINEERED MUTATION
SEQADV 3C0B ASP D 187 UNP Q6M145 ASN 187 ENGINEERED MUTATION
SEQADV 3C0B ASN D 254 UNP Q6M145 THR 254 ENGINEERED MUTATION
SEQADV 3C0B GLU D 268 UNP Q6M145 LYS 268 ENGINEERED MUTATION
SEQADV 3C0B ASN D 269 UNP Q6M145 LYS 269 ENGINEERED MUTATION
SEQADV 3C0B LEU D 284 UNP Q6M145 ILE 284 ENGINEERED MUTATION
SEQADV 3C0B ALA D 294 UNP Q6M145 GLY 294 ENGINEERED MUTATION
SEQADV 3C0B LEU D 327 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B GLU D 328 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS D 329 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS D 330 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS D 331 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS D 332 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS D 333 UNP Q6M145 EXPRESSION TAG
SEQADV 3C0B HIS D 334 UNP Q6M145 EXPRESSION TAG
SEQRES 1 A 334 MSE ILE LEU GLY ILE ASP ILE GLY GLY ALA ASN THR LYS
SEQRES 2 A 334 ILE THR GLU LEU HIS GLU ASN GLY GLU PHE LYS VAL HIS
SEQRES 3 A 334 HIS LEU TYR PHE PRO MSE TRP LYS ASN ASN ASP LYS LEU
SEQRES 4 A 334 ALA GLU VAL LEU LYS THR TYR SER ASN ASP VAL SER HIS
SEQRES 5 A 334 VAL ALA LEU VAL THR THR ALA GLU LEU ALA ASP SER TYR
SEQRES 6 A 334 GLU THR LYS LYS GLU GLY VAL ASP ASN ILE LEU ASN ALA
SEQRES 7 A 334 ALA GLU SER ALA PHE GLY SER ASN ILE SER VAL PHE ASP
SEQRES 8 A 334 SER ASN GLY ASN PHE ILE SER LEU GLU SER ALA LYS THR
SEQRES 9 A 334 ASN ASN MSE LYS VAL SER ALA SER ASN TRP CYS GLY THR
SEQRES 10 A 334 ALA LYS TRP VAL SER LYS ASN ILE GLU GLU ASN CYS ILE
SEQRES 11 A 334 LEU VAL ASP MSE GLY SER THR THR THR ASP ILE ILE PRO
SEQRES 12 A 334 ILE VAL GLU GLY LYS VAL VAL ALA GLU LYS THR ASP LEU
SEQRES 13 A 334 GLU ARG LEU MSE ASN HIS GLU LEU LEU TYR VAL GLY THR
SEQRES 14 A 334 LEU ARG THR PRO ILE SER HIS LEU GLY ASN THR ILE SER
SEQRES 15 A 334 PHE LYS GLY VAL ASP THR ASN VAL SER SER GLU TYR PHE
SEQRES 16 A 334 ALA ILE THR ALA ASP ILE SER VAL VAL LEU GLU LYS VAL
SEQRES 17 A 334 THR THR GLU GLU TYR THR CYS ASP THR PRO ASP GLY LYS
SEQRES 18 A 334 GLY THR ASP LYS ARG SER SER LEU VAL ARG ILE SER LYS
SEQRES 19 A 334 VAL LEU CYS SER ASP LEU ASP GLN ILE SER GLU ILE ASP
SEQRES 20 A 334 ALA GLU ASN ILE ALA LYS ASN TYR TYR GLU LEU TRP LYS
SEQRES 21 A 334 GLU LEU ILE LEU GLU ASN VAL GLU ASN VAL ALA GLU LYS
SEQRES 22 A 334 TYR GLY SER LYS LYS VAL VAL ILE THR GLY LEU GLY GLU
SEQRES 23 A 334 ASN ILE LEU LYS ASP ALA LEU ALA ASP PHE GLU VAL ILE
SEQRES 24 A 334 SER VAL ALA GLU ARG TYR GLY LYS ASP VAL SER LEU ALA
SEQRES 25 A 334 THR PRO SER PHE ALA VAL ALA GLU LEU LEU LYS ASN GLU
SEQRES 26 A 334 LEU LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 334 MSE ILE LEU GLY ILE ASP ILE GLY GLY ALA ASN THR LYS
SEQRES 2 B 334 ILE THR GLU LEU HIS GLU ASN GLY GLU PHE LYS VAL HIS
SEQRES 3 B 334 HIS LEU TYR PHE PRO MSE TRP LYS ASN ASN ASP LYS LEU
SEQRES 4 B 334 ALA GLU VAL LEU LYS THR TYR SER ASN ASP VAL SER HIS
SEQRES 5 B 334 VAL ALA LEU VAL THR THR ALA GLU LEU ALA ASP SER TYR
SEQRES 6 B 334 GLU THR LYS LYS GLU GLY VAL ASP ASN ILE LEU ASN ALA
SEQRES 7 B 334 ALA GLU SER ALA PHE GLY SER ASN ILE SER VAL PHE ASP
SEQRES 8 B 334 SER ASN GLY ASN PHE ILE SER LEU GLU SER ALA LYS THR
SEQRES 9 B 334 ASN ASN MSE LYS VAL SER ALA SER ASN TRP CYS GLY THR
SEQRES 10 B 334 ALA LYS TRP VAL SER LYS ASN ILE GLU GLU ASN CYS ILE
SEQRES 11 B 334 LEU VAL ASP MSE GLY SER THR THR THR ASP ILE ILE PRO
SEQRES 12 B 334 ILE VAL GLU GLY LYS VAL VAL ALA GLU LYS THR ASP LEU
SEQRES 13 B 334 GLU ARG LEU MSE ASN HIS GLU LEU LEU TYR VAL GLY THR
SEQRES 14 B 334 LEU ARG THR PRO ILE SER HIS LEU GLY ASN THR ILE SER
SEQRES 15 B 334 PHE LYS GLY VAL ASP THR ASN VAL SER SER GLU TYR PHE
SEQRES 16 B 334 ALA ILE THR ALA ASP ILE SER VAL VAL LEU GLU LYS VAL
SEQRES 17 B 334 THR THR GLU GLU TYR THR CYS ASP THR PRO ASP GLY LYS
SEQRES 18 B 334 GLY THR ASP LYS ARG SER SER LEU VAL ARG ILE SER LYS
SEQRES 19 B 334 VAL LEU CYS SER ASP LEU ASP GLN ILE SER GLU ILE ASP
SEQRES 20 B 334 ALA GLU ASN ILE ALA LYS ASN TYR TYR GLU LEU TRP LYS
SEQRES 21 B 334 GLU LEU ILE LEU GLU ASN VAL GLU ASN VAL ALA GLU LYS
SEQRES 22 B 334 TYR GLY SER LYS LYS VAL VAL ILE THR GLY LEU GLY GLU
SEQRES 23 B 334 ASN ILE LEU LYS ASP ALA LEU ALA ASP PHE GLU VAL ILE
SEQRES 24 B 334 SER VAL ALA GLU ARG TYR GLY LYS ASP VAL SER LEU ALA
SEQRES 25 B 334 THR PRO SER PHE ALA VAL ALA GLU LEU LEU LYS ASN GLU
SEQRES 26 B 334 LEU LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 334 MSE ILE LEU GLY ILE ASP ILE GLY GLY ALA ASN THR LYS
SEQRES 2 C 334 ILE THR GLU LEU HIS GLU ASN GLY GLU PHE LYS VAL HIS
SEQRES 3 C 334 HIS LEU TYR PHE PRO MSE TRP LYS ASN ASN ASP LYS LEU
SEQRES 4 C 334 ALA GLU VAL LEU LYS THR TYR SER ASN ASP VAL SER HIS
SEQRES 5 C 334 VAL ALA LEU VAL THR THR ALA GLU LEU ALA ASP SER TYR
SEQRES 6 C 334 GLU THR LYS LYS GLU GLY VAL ASP ASN ILE LEU ASN ALA
SEQRES 7 C 334 ALA GLU SER ALA PHE GLY SER ASN ILE SER VAL PHE ASP
SEQRES 8 C 334 SER ASN GLY ASN PHE ILE SER LEU GLU SER ALA LYS THR
SEQRES 9 C 334 ASN ASN MSE LYS VAL SER ALA SER ASN TRP CYS GLY THR
SEQRES 10 C 334 ALA LYS TRP VAL SER LYS ASN ILE GLU GLU ASN CYS ILE
SEQRES 11 C 334 LEU VAL ASP MSE GLY SER THR THR THR ASP ILE ILE PRO
SEQRES 12 C 334 ILE VAL GLU GLY LYS VAL VAL ALA GLU LYS THR ASP LEU
SEQRES 13 C 334 GLU ARG LEU MSE ASN HIS GLU LEU LEU TYR VAL GLY THR
SEQRES 14 C 334 LEU ARG THR PRO ILE SER HIS LEU GLY ASN THR ILE SER
SEQRES 15 C 334 PHE LYS GLY VAL ASP THR ASN VAL SER SER GLU TYR PHE
SEQRES 16 C 334 ALA ILE THR ALA ASP ILE SER VAL VAL LEU GLU LYS VAL
SEQRES 17 C 334 THR THR GLU GLU TYR THR CYS ASP THR PRO ASP GLY LYS
SEQRES 18 C 334 GLY THR ASP LYS ARG SER SER LEU VAL ARG ILE SER LYS
SEQRES 19 C 334 VAL LEU CYS SER ASP LEU ASP GLN ILE SER GLU ILE ASP
SEQRES 20 C 334 ALA GLU ASN ILE ALA LYS ASN TYR TYR GLU LEU TRP LYS
SEQRES 21 C 334 GLU LEU ILE LEU GLU ASN VAL GLU ASN VAL ALA GLU LYS
SEQRES 22 C 334 TYR GLY SER LYS LYS VAL VAL ILE THR GLY LEU GLY GLU
SEQRES 23 C 334 ASN ILE LEU LYS ASP ALA LEU ALA ASP PHE GLU VAL ILE
SEQRES 24 C 334 SER VAL ALA GLU ARG TYR GLY LYS ASP VAL SER LEU ALA
SEQRES 25 C 334 THR PRO SER PHE ALA VAL ALA GLU LEU LEU LYS ASN GLU
SEQRES 26 C 334 LEU LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 334 MSE ILE LEU GLY ILE ASP ILE GLY GLY ALA ASN THR LYS
SEQRES 2 D 334 ILE THR GLU LEU HIS GLU ASN GLY GLU PHE LYS VAL HIS
SEQRES 3 D 334 HIS LEU TYR PHE PRO MSE TRP LYS ASN ASN ASP LYS LEU
SEQRES 4 D 334 ALA GLU VAL LEU LYS THR TYR SER ASN ASP VAL SER HIS
SEQRES 5 D 334 VAL ALA LEU VAL THR THR ALA GLU LEU ALA ASP SER TYR
SEQRES 6 D 334 GLU THR LYS LYS GLU GLY VAL ASP ASN ILE LEU ASN ALA
SEQRES 7 D 334 ALA GLU SER ALA PHE GLY SER ASN ILE SER VAL PHE ASP
SEQRES 8 D 334 SER ASN GLY ASN PHE ILE SER LEU GLU SER ALA LYS THR
SEQRES 9 D 334 ASN ASN MSE LYS VAL SER ALA SER ASN TRP CYS GLY THR
SEQRES 10 D 334 ALA LYS TRP VAL SER LYS ASN ILE GLU GLU ASN CYS ILE
SEQRES 11 D 334 LEU VAL ASP MSE GLY SER THR THR THR ASP ILE ILE PRO
SEQRES 12 D 334 ILE VAL GLU GLY LYS VAL VAL ALA GLU LYS THR ASP LEU
SEQRES 13 D 334 GLU ARG LEU MSE ASN HIS GLU LEU LEU TYR VAL GLY THR
SEQRES 14 D 334 LEU ARG THR PRO ILE SER HIS LEU GLY ASN THR ILE SER
SEQRES 15 D 334 PHE LYS GLY VAL ASP THR ASN VAL SER SER GLU TYR PHE
SEQRES 16 D 334 ALA ILE THR ALA ASP ILE SER VAL VAL LEU GLU LYS VAL
SEQRES 17 D 334 THR THR GLU GLU TYR THR CYS ASP THR PRO ASP GLY LYS
SEQRES 18 D 334 GLY THR ASP LYS ARG SER SER LEU VAL ARG ILE SER LYS
SEQRES 19 D 334 VAL LEU CYS SER ASP LEU ASP GLN ILE SER GLU ILE ASP
SEQRES 20 D 334 ALA GLU ASN ILE ALA LYS ASN TYR TYR GLU LEU TRP LYS
SEQRES 21 D 334 GLU LEU ILE LEU GLU ASN VAL GLU ASN VAL ALA GLU LYS
SEQRES 22 D 334 TYR GLY SER LYS LYS VAL VAL ILE THR GLY LEU GLY GLU
SEQRES 23 D 334 ASN ILE LEU LYS ASP ALA LEU ALA ASP PHE GLU VAL ILE
SEQRES 24 D 334 SER VAL ALA GLU ARG TYR GLY LYS ASP VAL SER LEU ALA
SEQRES 25 D 334 THR PRO SER PHE ALA VAL ALA GLU LEU LEU LYS ASN GLU
SEQRES 26 D 334 LEU LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 3C0B MSE A 1 MET SELENOMETHIONINE
MODRES 3C0B MSE A 32 MET SELENOMETHIONINE
MODRES 3C0B MSE A 134 MET SELENOMETHIONINE
MODRES 3C0B MSE A 160 MET SELENOMETHIONINE
MODRES 3C0B MSE B 1 MET SELENOMETHIONINE
MODRES 3C0B MSE B 107 MET SELENOMETHIONINE
MODRES 3C0B MSE B 134 MET SELENOMETHIONINE
MODRES 3C0B MSE B 160 MET SELENOMETHIONINE
MODRES 3C0B MSE C 1 MET SELENOMETHIONINE
MODRES 3C0B MSE C 32 MET SELENOMETHIONINE
MODRES 3C0B MSE C 107 MET SELENOMETHIONINE
MODRES 3C0B MSE C 134 MET SELENOMETHIONINE
MODRES 3C0B MSE C 160 MET SELENOMETHIONINE
MODRES 3C0B MSE D 1 MET SELENOMETHIONINE
MODRES 3C0B MSE D 32 MET SELENOMETHIONINE
MODRES 3C0B MSE D 107 MET SELENOMETHIONINE
MODRES 3C0B MSE D 134 MET SELENOMETHIONINE
MODRES 3C0B MSE D 160 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 32 8
HET MSE A 134 8
HET MSE A 160 8
HET MSE B 1 8
HET MSE B 107 8
HET MSE B 134 8
HET MSE B 160 8
HET MSE C 1 8
HET MSE C 32 8
HET MSE C 107 8
HET MSE C 134 8
HET MSE C 160 8
HET MSE D 1 8
HET MSE D 32 8
HET MSE D 107 8
HET MSE D 134 8
HET MSE D 160 8
HET CA B 402 1
HET CA D 401 1
HETNAM MSE SELENOMETHIONINE
HETNAM CA CALCIUM ION
FORMUL 1 MSE 18(C5 H11 N O2 SE)
FORMUL 5 CA 2(CA 2+)
FORMUL 7 HOH *160(H2 O)
HELIX 1 1 ALA A 40 LYS A 44 5 5
HELIX 2 2 VAL A 72 GLY A 84 1 13
HELIX 3 3 LEU A 99 ASN A 105 1 7
HELIX 4 4 TRP A 114 ILE A 125 1 12
HELIX 5 5 THR A 154 MSE A 160 1 7
HELIX 6 6 PRO A 173 GLY A 178 5 6
HELIX 7 7 ILE A 197 LEU A 205 1 9
HELIX 8 8 THR A 209 TYR A 213 5 5
HELIX 9 9 ASP A 224 VAL A 235 1 12
HELIX 10 10 SER A 244 GLY A 275 1 32
HELIX 11 11 GLY A 285 LEU A 293 1 9
HELIX 12 12 VAL A 301 GLY A 306 1 6
HELIX 13 13 GLY A 306 LEU A 311 1 6
HELIX 14 14 ALA A 312 LEU A 327 1 16
HELIX 15 15 ASN B 35 VAL B 42 1 8
HELIX 16 16 GLY B 71 GLY B 84 1 14
HELIX 17 17 TRP B 114 ILE B 125 1 12
HELIX 18 18 THR B 154 ASN B 161 1 8
HELIX 19 19 PRO B 173 GLY B 178 1 6
HELIX 20 20 ILE B 197 LEU B 205 1 9
HELIX 21 21 THR B 209 TYR B 213 5 5
HELIX 22 22 ASP B 224 LYS B 234 1 11
HELIX 23 23 VAL B 235 CYS B 237 5 3
HELIX 24 24 SER B 244 GLY B 275 1 32
HELIX 25 25 GLY B 285 LEU B 293 1 9
HELIX 26 26 VAL B 301 TYR B 305 1 5
HELIX 27 27 GLY B 306 LEU B 311 1 6
HELIX 28 28 ALA B 312 HIS B 330 1 19
HELIX 29 29 ALA C 40 LYS C 44 5 5
HELIX 30 30 VAL C 72 GLY C 84 1 13
HELIX 31 31 GLU C 100 ASN C 105 1 6
HELIX 32 32 TRP C 114 ILE C 125 1 12
HELIX 33 33 THR C 154 MSE C 160 1 7
HELIX 34 34 PRO C 173 GLY C 178 5 6
HELIX 35 35 ILE C 197 LEU C 205 1 9
HELIX 36 36 THR C 209 TYR C 213 5 5
HELIX 37 37 ASP C 224 VAL C 235 1 12
HELIX 38 38 SER C 244 GLY C 275 1 32
HELIX 39 39 GLY C 285 LEU C 293 1 9
HELIX 40 40 VAL C 301 GLY C 306 1 6
HELIX 41 41 GLY C 306 LEU C 311 1 6
HELIX 42 42 ALA C 312 GLU C 328 1 17
HELIX 43 43 LEU D 39 LYS D 44 5 6
HELIX 44 44 VAL D 72 GLY D 84 1 13
HELIX 45 45 LEU D 99 THR D 104 1 6
HELIX 46 46 TRP D 114 ILE D 125 1 12
HELIX 47 47 THR D 154 ASN D 161 1 8
HELIX 48 48 PRO D 173 GLY D 178 5 6
HELIX 49 49 ILE D 197 LEU D 205 1 9
HELIX 50 50 THR D 209 TYR D 213 5 5
HELIX 51 51 ASP D 224 LYS D 234 1 11
HELIX 52 52 VAL D 235 CYS D 237 5 3
HELIX 53 53 SER D 244 GLY D 275 1 32
HELIX 54 54 GLY D 285 LEU D 293 1 9
HELIX 55 55 VAL D 301 GLY D 306 1 6
HELIX 56 56 GLY D 306 LEU D 311 1 6
HELIX 57 57 ALA D 312 LEU D 327 1 16
SHEET 1 A 6 PHE A 23 TYR A 29 0
SHEET 2 A 6 ASN A 11 LEU A 17 -1 N ILE A 14 O HIS A 26
SHEET 3 A 6 ILE A 2 GLY A 8 -1 N ILE A 2 O LEU A 17
SHEET 4 A 6 VAL A 50 ALA A 54 1 O SER A 51 N ILE A 5
SHEET 5 A 6 ILE A 87 PHE A 90 1 O PHE A 90 N HIS A 52
SHEET 6 A 6 PHE A 96 SER A 98 -1 O ILE A 97 N VAL A 89
SHEET 1 B 3 LYS A 148 VAL A 149 0
SHEET 2 B 3 THR A 139 VAL A 145 -1 N VAL A 145 O LYS A 148
SHEET 3 B 3 LEU A 164 LEU A 165 -1 O LEU A 165 N THR A 139
SHEET 1 C 5 LYS A 148 VAL A 149 0
SHEET 2 C 5 THR A 139 VAL A 145 -1 N VAL A 145 O LYS A 148
SHEET 3 C 5 CYS A 129 MSE A 134 -1 N CYS A 129 O ILE A 144
SHEET 4 C 5 LYS A 278 THR A 282 1 O VAL A 280 N VAL A 132
SHEET 5 C 5 GLU A 297 SER A 300 1 O ILE A 299 N VAL A 279
SHEET 1 D 2 THR A 180 PHE A 183 0
SHEET 2 D 2 VAL A 186 ASN A 189 -1 O THR A 188 N ILE A 181
SHEET 1 E 6 PHE B 23 TYR B 29 0
SHEET 2 E 6 ASN B 11 LEU B 17 -1 N GLU B 16 O LYS B 24
SHEET 3 E 6 ILE B 2 ILE B 7 -1 N ASP B 6 O LYS B 13
SHEET 4 E 6 ASP B 49 ALA B 54 1 O SER B 51 N LEU B 3
SHEET 5 E 6 ILE B 87 PHE B 90 1 O SER B 88 N VAL B 50
SHEET 6 E 6 PHE B 96 SER B 98 -1 O ILE B 97 N VAL B 89
SHEET 1 F 3 LYS B 148 VAL B 149 0
SHEET 2 F 3 THR B 139 VAL B 145 -1 N VAL B 145 O LYS B 148
SHEET 3 F 3 LEU B 164 LEU B 165 -1 O LEU B 165 N THR B 139
SHEET 1 G 5 LYS B 148 VAL B 149 0
SHEET 2 G 5 THR B 139 VAL B 145 -1 N VAL B 145 O LYS B 148
SHEET 3 G 5 CYS B 129 MSE B 134 -1 N CYS B 129 O ILE B 144
SHEET 4 G 5 LYS B 278 THR B 282 1 O VAL B 280 N VAL B 132
SHEET 5 G 5 GLU B 297 SER B 300 1 O ILE B 299 N VAL B 279
SHEET 1 H 2 THR B 180 PHE B 183 0
SHEET 2 H 2 VAL B 186 ASN B 189 -1 O THR B 188 N ILE B 181
SHEET 1 I 6 PHE C 23 TYR C 29 0
SHEET 2 I 6 ASN C 11 LEU C 17 -1 N GLU C 16 O LYS C 24
SHEET 3 I 6 ILE C 2 ILE C 7 -1 N ILE C 2 O LEU C 17
SHEET 4 I 6 ASP C 49 ALA C 54 1 O SER C 51 N ILE C 5
SHEET 5 I 6 ILE C 87 PHE C 90 1 O PHE C 90 N HIS C 52
SHEET 6 I 6 PHE C 96 SER C 98 -1 O ILE C 97 N VAL C 89
SHEET 1 J 3 LYS C 148 VAL C 149 0
SHEET 2 J 3 THR C 139 VAL C 145 -1 N VAL C 145 O LYS C 148
SHEET 3 J 3 LEU C 164 LEU C 165 -1 O LEU C 165 N THR C 139
SHEET 1 K 5 LYS C 148 VAL C 149 0
SHEET 2 K 5 THR C 139 VAL C 145 -1 N VAL C 145 O LYS C 148
SHEET 3 K 5 CYS C 129 MSE C 134 -1 N LEU C 131 O ILE C 142
SHEET 4 K 5 LYS C 278 THR C 282 1 O VAL C 280 N VAL C 132
SHEET 5 K 5 GLU C 297 SER C 300 1 O ILE C 299 N VAL C 279
SHEET 1 L 2 THR C 180 PHE C 183 0
SHEET 2 L 2 VAL C 186 ASN C 189 -1 O THR C 188 N ILE C 181
SHEET 1 M 6 PHE D 23 TYR D 29 0
SHEET 2 M 6 ASN D 11 LEU D 17 -1 N GLU D 16 O LYS D 24
SHEET 3 M 6 ILE D 2 ILE D 7 -1 N ILE D 2 O LEU D 17
SHEET 4 M 6 ASP D 49 ALA D 54 1 O SER D 51 N LEU D 3
SHEET 5 M 6 ILE D 87 PHE D 90 1 O PHE D 90 N HIS D 52
SHEET 6 M 6 PHE D 96 SER D 98 -1 O ILE D 97 N VAL D 89
SHEET 1 N 3 LYS D 148 VAL D 149 0
SHEET 2 N 3 THR D 139 VAL D 145 -1 N VAL D 145 O LYS D 148
SHEET 3 N 3 LEU D 164 LEU D 165 -1 O LEU D 165 N THR D 139
SHEET 1 O 5 LYS D 148 VAL D 149 0
SHEET 2 O 5 THR D 139 VAL D 145 -1 N VAL D 145 O LYS D 148
SHEET 3 O 5 CYS D 129 MSE D 134 -1 N LEU D 131 O ILE D 142
SHEET 4 O 5 LYS D 278 THR D 282 1 O VAL D 280 N VAL D 132
SHEET 5 O 5 GLU D 297 SER D 300 1 O GLU D 297 N VAL D 279
SHEET 1 P 2 THR D 180 PHE D 183 0
SHEET 2 P 2 VAL D 186 ASN D 189 -1 O THR D 188 N ILE D 181
LINK C MSE A 1 N ILE A 2 1555 1555 1.33
LINK C PRO A 31 N MSE A 32 1555 1555 1.33
LINK C ASP A 133 N MSE A 134 1555 1555 1.33
LINK C MSE A 134 N GLY A 135 1555 1555 1.33
LINK C LEU A 159 N MSE A 160 1555 1555 1.33
LINK C MSE A 160 N ASN A 161 1555 1555 1.33
LINK C MSE B 1 N ILE B 2 1555 1555 1.33
LINK C ASN B 106 N MSE B 107 1555 1555 1.33
LINK C MSE B 107 N LYS B 108 1555 1555 1.33
LINK C ASP B 133 N MSE B 134 1555 1555 1.33
LINK C MSE B 134 N GLY B 135 1555 1555 1.33
LINK C LEU B 159 N MSE B 160 1555 1555 1.33
LINK C MSE B 160 N ASN B 161 1555 1555 1.33
LINK C MSE C 1 N ILE C 2 1555 1555 1.33
LINK C PRO C 31 N MSE C 32 1555 1555 1.33
LINK C ASN C 106 N MSE C 107 1555 1555 1.33
LINK C MSE C 107 N LYS C 108 1555 1555 1.33
LINK C ASP C 133 N MSE C 134 1555 1555 1.33
LINK C MSE C 134 N GLY C 135 1555 1555 1.33
LINK C LEU C 159 N MSE C 160 1555 1555 1.33
LINK C MSE C 160 N ASN C 161 1555 1555 1.33
LINK C MSE D 1 N ILE D 2 1555 1555 1.33
LINK C PRO D 31 N MSE D 32 1555 1555 1.33
LINK C ASN D 106 N MSE D 107 1555 1555 1.32
LINK C MSE D 107 N LYS D 108 1555 1555 1.33
LINK C ASP D 133 N MSE D 134 1555 1555 1.33
LINK C MSE D 134 N GLY D 135 1555 1555 1.33
LINK C LEU D 159 N MSE D 160 1555 1555 1.33
LINK C MSE D 160 N ASN D 161 1555 1555 1.33
LINK OE1 GLU B 152 CA CA B 402 1555 1555 2.92
LINK OE1 GLU D 152 CA CA D 401 1555 1555 2.89
SITE 1 AC1 2 GLU B 146 GLU D 152
SITE 1 AC2 2 GLU B 152 GLU D 146
CRYST1 157.400 87.266 123.988 90.00 110.29 90.00 C 1 2 1 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006353 0.000000 0.002349 0.00000
SCALE2 0.000000 0.011459 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008599 0.00000
HETATM 1 N MSE A 1 57.322 7.148 28.285 1.00 67.03 N
HETATM 2 CA MSE A 1 57.312 6.916 26.812 1.00 66.47 C
HETATM 3 C MSE A 1 55.866 6.939 26.324 1.00 63.54 C
HETATM 4 O MSE A 1 55.070 6.081 26.695 1.00 63.51 O
HETATM 5 CB MSE A 1 57.956 5.559 26.504 1.00 90.30 C
HETATM 6 CG MSE A 1 58.769 5.501 25.209 1.00 96.84 C
HETATM 7 SE MSE A 1 57.761 5.272 23.566 1.00105.80 SE
HETATM 8 CE MSE A 1 57.905 3.349 23.375 1.00102.58 C
(ATOM LINES ARE NOT SHOWN.)
END
